Research workbench
AlphaFold monomer V2.0 prediction for polyribonucleotide nucleotidyltransferase (Q18BI4)
Analyse AlphaFold monomer V2.0 prediction for polyribonucleotide nucleotidyltransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q18BI4
- Type
- protein
- Length
- 703 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5BeA89782341f98147F2D811B063F91F0aE7D7bF
- Molecule
- Polyribonucleotide nucleotidyltransferase
- UniProt
- Q18BI4
- Pockets
- 3 · best druggability 0.75
Structure
1 distinct chain · 35% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyribonucleotide nucleotidyltransferase | protein | 703 | 35% helix, 30% strand | Q18BI4 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 802 | 0.75 | 0.79 | 87 | empty |
| 2 | 1059 | 0.72 | 0.76 | 83 | empty |
| 3 | 60 | 0.35 | 0.78 | 15 | empty |
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q18BI4
- Elsewhere: UniProt Q18BI4 · AlphaFold DB Q18BI4
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